ID   BR2E_RANES              Reviewed;          33 AA.
AC   P32413;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   22-JUL-2008, entry version 36.
DE   RecName: Full=Brevinin-2E;
OS   Rana esculenta (Edible frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana;
OC   Pelophylax.
OX   NCBI_TaxID=8401;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion;
RX   MEDLINE=93285327; PubMed=8508915; DOI=10.1016/0014-5793(93)81384-C;
RA   Simmaco M., Mignogna G., Barra D., Bossa F.;
RT   "Novel antimicrobial peptides from skin secretion of the European frog
RT   Rana esculenta.";
RL   FEBS Lett. 324:159-161(1993).
CC   -!- FUNCTION: Shows antibacterial activity against representative
CC       Gram-negative and Gram-positive bacterial species, and hemolytic
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; S33730; S33730.
DR   HOVERGEN; P32413; -.
DR   InterPro; IPR012521; Antimicrobial_2.
DR   Pfam; PF08023; Antimicrobial_2; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Hemolysis; Secreted.
FT   PEPTIDE       1     33       Brevinin-2E.
FT                                /FTId=PRO_0000044642.
FT   DISULFID     27     33
SQ   SEQUENCE   33 AA;  3364 MW;  99140BC640ABB0EE CRC64;
     GIMDTLKNLA KTAGKGALQS LLNKASCKLS GQC
//